The CydDC family of ABC transporters export the low molecular weight thiols glutathione and cysteine to the periplasm of a variety of bacterial species. The CydDC complex has previously been shown to be important for disulfide folding, motility, respiration, and tolerance to nitric oxide and antibiotics. In addition, CydDC is thus far unique amongst ABC transporters in that it binds a haem cofactor that appears to modulate ATPase activity. CydDC has a diverse impact upon bacterial metabolism, growth, and virulence, and is of interest to those working on membrane transport mechanisms, redox biology, aerobic respiration, and stress sensing/tolerance during infection.
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The CydDC family of transporters.
Res Microbiol
January 2020
School of Biosciences, University of Kent, Canterbury, United Kingdom. Electronic address:
The CydDC family of ABC transporters export the low molecular weight thiols glutathione and cysteine to the periplasm of a variety of bacterial species. The CydDC complex has previously been shown to be important for disulfide folding, motility, respiration, and tolerance to nitric oxide and antibiotics. In addition, CydDC is thus far unique amongst ABC transporters in that it binds a haem cofactor that appears to modulate ATPase activity.
View Article and Find Full Text PDFThe CydDC Family of Transporters and Their Roles in Oxidase Assembly and Homeostasis.
Adv Microb Physiol
April 2016
School of Biosciences, University of Kent, Canterbury, United Kingdom. Electronic address:
The CydDC complex of Escherichia coli is a heterodimeric ATP-binding cassette type transporter (ABC transporter) that exports the thiol-containing redox-active molecules cysteine and glutathione. These reductants are thought to aid redox homeostasis of the periplasm, permitting correct disulphide folding of periplasmic and secreted proteins. Loss of CydDC results in the periplasm becoming more oxidising and abolishes the assembly of functional bd-type respiratory oxidases that couple the oxidation of ubiquinol to the reduction of oxygen to water.
View Article and Find Full Text PDFThe cydD gene product, component of a heterodimeric ABC transporter, is required for assembly of periplasmic cytochrome c and of cytochrome bd in Escherichia coli.
FEMS Microbiol Lett
April 1994
Division of Biochemistry and Molecular Biology, John Curtin School of Medical Research, Australian National University, Canberra City, ACT.
The cydD gene of Escherichia coli encodes a protein which, together with the CydC protein, probably constitutes a heterodimeric, ABC-family membrane transporter, necessary for biosynthesis of the cytochrome bd quinol oxidase. Here, we demonstrate that a cydD mutant also fails to synthesise periplasmic c-type cytochrome(s), suggesting that the transporter exports haem or some other component involved in assembly of cytochromes that are found in, or exposed to, the periplasm. The CydDC system appears to be the first example of a transporter required for periplasmic cytochrome assembly processes requiring more than one type of haem.
View Article and Find Full Text PDFCytochrome bd biosynthesis in Escherichia coli: the sequences of the cydC and cydD genes suggest that they encode the components of an ABC membrane transporter.
Mol Microbiol
October 1993
Microbial Physiology and Environmental Biotechnology Group, Division of Life Sciences, King's College London, Campden Hill Road, London W8 7AH, UK.Division of Biochemistry and Molecular Biology, John Curtin School of Medical Research, Australian National University, Canberra, ACT 2601, Australia.
At least four genes are known to affect formation of the cytochrome bd-type terminal oxidase of Escherichia coli. In addition to the genes (cydA and cydB) encoding the two constituent subunits of this complex, a further two genes (cydC and cydD) map near 19 min on the E. coli chromosome.
View Article and Find Full Text PDFCytochrome bd biosynthesis in Escherichia coli: the sequences of the cydC and cydD genes suggest that they encode the components of an ABC membrane transporter.
Mol Microbiol
October 1993
Division of Life Sciences, King's College London, UK.
At least four genes are known to affect formation of the cytochrome bd-type terminal oxidase of Escherichia coli. In addition to the genes (cydA and cydB) encoding the two constituent subunits of this complex, a further two genes (cydC and cydD) map near 19 min on the E. coli chromosome.
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